@article {2910,
	title = {FLUORESCENT RESPONSES OF ACRYLODAN-LABELED PLASMA GELSOLIN},
	journal = {Archives of Biochemistry and Biophysics},
	volume = {302},
	number = {1},
	year = {1993},
	note = {ISI Document Delivery No.: KW472Times Cited: 12Cited Reference Count: 24},
	month = {Apr},
	pages = {31-36},
	type = {Article},
	keywords = {ACTIN-BINDING DOMAIN, FILAMENTS, PROTEINS},
	isbn = {0003-9861},
	url = {<Go to ISI>://A1993KW47200005},
	author = {Reid, S. W. and Koepf, E. K. and Burtnick, L. D.}
}
@article {2845,
	title = {HORSE PLASMA GELSOLIN LABELED WITH FLUORESCEIN ISOTHIOCYANATE RESPONDS TO CALCIUM AND ACTIN},
	journal = {European Journal of Biochemistry},
	volume = {212},
	number = {3},
	year = {1993},
	note = {ISI Document Delivery No.: KT704Times Cited: 7Cited Reference Count: 26},
	month = {Mar},
	pages = {713-718},
	type = {Article},
	abstract = {Reaction between horse plasma gelsolin and fluorescein-5-isothiocyanate (FITC) resulted in incorporation of 4.8 +/- 0.6 fluorescein groups/gelsolin molecule. The sites of modification were not clustered in any one portion of the gelsolin polypeptide chain; all major peptides produced by proteolytic digestion with alpha-chymotrypsin exhibited a fluorescence characteristic of fluorescein. FITC-gelsolin has a peptide-backbone circular dichroism spectrum at 20-degrees-C that is indistinguishable from that of native gelsolin, but FITC-gelsolin is considerably more resistant than native gelsolin to thermally induced precipitation. FITC-gelsolin is fully able to carry out severing of F-actin filaments, the prime function of gelsolin in plasma. An opening up of the structure of gelsolin on binding Ca2+ is evident from an increased susceptibility of FITC-gelsolin to quenching by I-. Ca2+ dependence of the interaction between gelsolin and actin is evident in titrations both of intensity and polarization of the fluorescence of FITC-gelsolin solutions. A Ca2+-sensitive interaction between gelsolin and tropomyosin also is observed.},
	keywords = {BINDING DOMAIN, FILAMENTS, PROTEIN, TROPOMYOSIN},
	isbn = {0014-2956},
	url = {<Go to ISI>://A1993KT70400010},
	author = {Koepf, E. K. and Burtnick, L. D.}
}
@article {7284,
	title = {INTERACTION OF PLASMA GELSOLIN WITH TROPOMYOSIN},
	journal = {Febs Letters},
	volume = {309},
	number = {1},
	year = {1992},
	note = {ISI Document Delivery No.: JL068Times Cited: 20Cited Reference Count: 17},
	month = {Aug},
	pages = {56-58},
	type = {Article},
	abstract = {Horse plasma gelsolin labelled with benzophenone-4-isothiocyanate can be photochemically cross-linked to rabbit cardiac tropomyosin. The cross-linking proceeds with greater efficiency in calcium-containing buffers. Further evidence for interaction between these proteins is provided by retention of fluorescently labelled gelsolin on tropomyosin-agarose affinity columns and by the ability of tropomyosin to cause an increase in the fluorescence intensity of gelsolin labelled with fluorescein-5-isothiocyanate. Both of these effects require the presence of calcium ions.},
	keywords = {actin, FILAMENTS, gelsolin, MUSCLE, PROTEIN, TROPOMYOSIN},
	isbn = {0014-5793},
	url = {<Go to ISI>://A1992JL06800013},
	author = {Koepf, E. K. and Burtnick, L. D.}
}
